Recombinant Human Histone deacetylase 1(HDAC1)

Code CSB-EP010235HU
Size $1812Purchase it in Cusabio online store
(only available for customers from the US)
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP010235HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HDAC1.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP010235HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HDAC1.
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Product Details

Description

In the production of recombinant Human HDAC1 protein, the gene for HDAC1 (E.coli) was cloned into a vector and expressed as HDAC1 protein in E.coli. The plasmids with the copy of HDAC1, or the expression vector, were often used to enhance gene expression. Every step of production was undergone with a strict QC system. N-terminal 6xHis-SUMO tag was used in the process. The purity is 90% determined by SDS-PAGE. And the activity has been validated.

HDAC1 belongs to the class IV family. HDAC1 is found in at least three evolutionally conserved, distinct protein complexes: the Sin3, the CoREST and the Mi-2/NuRD complexes. HDAC1 activity is modulated through various post translational modifications including phosphorylation, acetylation, ubiquitination, sumoylation, and nitrosylation. HDAC1 is phosphorylated at serine 421 and 423 by casein kinase II and dephosphorylated by mitogen-activated protein kinase phosphatase-3 (MKP-3). Mutagenesis analysis suggested that phosphorylation on these sites are important for histone deacetylase activity and for HDAC1 to interact with corepressor complexes. HDAC1 phosphorylation increases during the G1 phase and was significantly reduced during the late S/G2 phase. Clinically, it has been shown HDACi can reactivate fetal globin in adult erythroid cells, suggesting the role of HDAC1 in modulating key transcription factors for erythropoiesis and its clinical relevance.

Purity Greater than 90% as determined by SDS-PAGE.
Target Names HDAC1
Uniprot No. Q13547
Research Area Immunology
Alternative Names DKFZp686H12203; GON 10; HD1; HDAC 1; HDAC1; HDAC1_HUMAN; Histone deacetylase 1; Reduced potassium dependency yeast homolog like 1; RPD3; RPD3L1
Species Homo sapiens (Human)
Source E.coli
Expression Region 1-482aa
Target Protein Sequence MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 71.1kDa
Protein Length Full Length
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

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Target Background

Function
(From Uniprot)
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation.
Gene References into Functions
  1. HDAC1,2 inhibitor either alone or when combined with doxorubicin decreases leukemia burden. PMID: 28579617
  2. miR-34a exhibited suppressive effects on ovarian cancer (OC) cells via directly binding and downregulating HDAC1 expression, which subsequently decreased the resistance to cisplatin and suppressed proliferation in OC cells. PMID: 29561664
  3. Study identified HDAC1, a key regulator of eukaryotic gene expression and many important cellular events, including cell proliferation, differentiation, cancer and immunity, as an interacting partner of ABIN1. PMID: 29058807
  4. r meta-analysis demonstrated an association between increased HDAC1 expression and better OS in Asian breast cancer patients PMID: 29738697
  5. Daxx directly binds to the DNA-binding domain of Slug, impeding histone deacetylase 1 (HDAC1) recruitment and antagonizing Slug E-box binding. This, in turn, stimulates E-cadherin and occludin expression and suppresses Slug-mediated epithelial-mesenchymal transition (EMT) and cell invasiveness. PMID: 28004751
  6. the knockdown of HDAC1/2 upregulated KLF5 protein but not KLF5 mRNA, and the increase in KLF5 protein level by silencing HDAC1/2 was at least in part due to decreased proteasomal degradation. PMID: 29679567
  7. HDAC1 knockdown by siRNA suppressed cell proliferation, and increased apoptosis and chemosensitivity by downregulating c-Myc and upregulating miR-34a. PMID: 30071534
  8. The HDAC1 expression was associated with the SNAIL expression in clinical samples. PMID: 29917299
  9. data show that Hdac1 and Hdac2 impact on Emu-myc B cell proliferation and apoptosis and suggest that a critical level of Hdac activity may be required for Emu-myc tumorigenesis and proper B cell development PMID: 27886239
  10. Data show there is allosteric communication between the inositol-binding site and the active sites in histone deacetylases HDAC1 and HDAC3. PMID: 27109927
  11. High HDAC1 expression is associated with gastrointestinal malignancy. PMID: 28424407
  12. Results show that proteasomal degradation of HDAC1 and HDAC3 by Vpr counteracts HIV-1 latency to reactivate the viral promoter. PMID: 27550312
  13. concomitant LSD1 and HDAC inhibition synergistically induces cell death in rhabdomyosarcoma cells by shifting the ratio of pro- and antiapoptotic BCL-2 proteins in favor of apoptosis, thereby engaging the intrinsic apoptotic pathway PMID: 28617441
  14. Hdac1 levels are increased in blood samples from patients with schizophrenia who had encountered early life stress (ELS), compared with patients without ELS experience. PMID: 28533418
  15. HDAC1 and HDAC2 suppress the expression of PPP2R3A/PR130, a regulatory subunit of the trimeric serine/threonine phosphatase 2 (PP2A). PMID: 29472538
  16. HDAC1 may therefore be considered an unfavorable progression indicator for glioma patients, and may also serve as a potential therapeutic target. PMID: 28624794
  17. new basis of DDX23-Linc00630-HDAC1 signal axis for understanding its pathogenicity, which could be further developed as a valuable therapeutic strategy PMID: 28473661
  18. Results show that histone deacetylase 1 (HDAC1) expression was positively correlated with YY1 transcription factor (YY1) in hepatocellular carcinoma (HCC) cell lines and primary tumor tissues. PMID: 28489564
  19. the combination of p63-positive and HDAC1-negative expressions can be a potential new way for distinguishing epidermal stem cells. PMID: 28672879
  20. Nuclear HDAC2 immunopositivity was significantly higher in actinic cheilitis (AC) when compared with lip squamous cell carcinoma (LSCC). HDAC1 and HAT1 nuclear immunostaining were higher in AC, with no statistical significance. When comparing data with our previous study, we found a positive correlation between HDAC1 X DNMT1/DNMT3b, HDAC2 X DNMT3b, and HAT1 X DNMT1/DNMT3b for certain studied groups. PMID: 28107582
  21. data reveal the mechanism by which chromatin remodeling and target gene expression are regulated by Ikaros alone and in complex with HDAC1 in B-ALL PMID: 26639180
  22. Histone deacetylases 1 and 2 cooperate in regulating BRCA1, CHK1, and RAD51 expression in acute myeloid leukemia cells. PMID: 28030834
  23. our findings identify a key role for c-Myc in TRAIL deregulation and as a biomarker of the anticancer action of HDACi in acute myeloid leukemia . PMID: 27358484
  24. The authors found that 2-aminoacetophenone regulates histone deacetylase 1 expression and activity, resulting in hypo-acetylation of lysine 18 of histone H3 at pro-inflammatory cytokine loci. Specifically, 2-aminoacetophenone induced reprogramming of immune cells occurs via alterations in histone acetylation of immune cytokines in vivo and in vitro. PMID: 27694949
  25. Histone deacetylases (HDACs) inhibitor MGCD0103 (MGCD) induces apoptosis by up-regulating p53 in CNE2 nasopharyngeal carcinoma (NPC) cells. PMID: 27283770
  26. Our findings suggest that up-regulation of UVRAG by HDAC1 inhibition potentiates DNA-damage-mediated cell death in colorectal cancer cells PMID: 29277783
  27. The findings suggest that OGT promotes the O-GlcNAc modification of HDAC1 in the development of progression hepatocellular carcinoma. PMID: 27060025
  28. HDAC1 promoted migration and invasion of gallbladder tumor cells by binding with TCF12 to promote epithelial mesenchymal transformation. PMID: 27092878
  29. HDAC1 depletion-induced p53 expression alters cardiac-derived mesenchymal stromal cell fate decisions. PMID: 27501845
  30. These results are the first evidence that the inhibition of HDAC1 by (S)-2 downregulates CIP2A transcription PMID: 27029072
  31. data showed that HDAC1 can trigger the proliferation and migration of breast cancer cells via activation of Snail/IL-8 signals PMID: 28779562
  32. Mechanical stimulation orchestrates the osteogenic differentiation of human bone marrow stromal cells by regulating HDAC1 PMID: 27171263
  33. High HDAC1 expression is associated with Multidrug Resistance in breast and cervical cancer. PMID: 28716899
  34. these results suggest that HDAC1 and HDAC6 may play a role in clear cell renal cell carcinoma biology PMID: 27506904
  35. Histone deacetylase 1 regulates the expression of progesterone receptor A during human parturition by occupying the progesterone receptor A promoter. PMID: 26758364
  36. High HDAC1 expression may contribute to the aggressiveness of human breast cancer with cytoplasmic-only expression of maspin PMID: 28870936
  37. Results indicate that HCV core induced epithelial-mesenchymal transition (EMT) by interacting with the transcriptional repressor complex Snail/HDAC1/2 at the E-cadherin promoter, which led to E-cadherin repression and increased invasiveness of hepatoma cells. PMID: 26549030
  38. Coexpression of SALL4 with HDAC1 and/or HDAC2 was associated with PTEN underexpression and a poor prognosis in hepatocellular carcinoma. PMID: 28411180
  39. Acetylation-dependent control of global poly(A) RNA degradation by CBP/p300 and HDAC1-HDAC2 has been described. PMID: 27635759
  40. Meta-analysis results suggest that HDAC1 mRNA or protein expression may serve as a good diagnostic and prognostic marker for lung cancer. PMID: 28767587
  41. Histone deacetylase assays confirmed that MIER2, but not MIER3 complexes, have associated deacetylase activity. PMID: 28046085
  42. High HDAC1 expression is associated with drug Resistance in Malignant Melanoma. PMID: 26980768
  43. HDAC1 overexpression is associated with Breast Cancer. PMID: 27197203
  44. Data suggest that epigenetic changes in histone acetylation and DNA methylation may contribute to the repression of RGS2 (regulator of G-protein signaling 2) expression in chemo-resistant ovarian cancer cells; regulation of HDAC1 (histone deacetylase 1) and DNMT1 (DNA methyltransferase 1) contribute to the suppression of RGS2. PMID: 28102109
  45. class I HDACs (HDAC1, 2, 3 and 8) play a major role in regulating extracellular matrix and Epithelial-mesenchymal transition, whereas class IIa HDACs (HDAC4 and 5) are less effective. PMID: 27420561
  46. We found that TCF7L1 recruits the C-terminal binding protein (CtBP) and histone deacetylase 1 (HDAC1) to the DKK4 promoter to repress DKK4 gene expression. In the absence of TCF7L1, TCF7L2 and beta-catenin occupancy at the DKK4 promoter is stimulated and DKK4 expression is increased. These findings uncover a critical role for TCF7L1 in repressing DKK4 gene expression to promote the oncogenic potential of CRCs. PMID: 28450117
  47. Using mass spectrometry and site directed mutagenesis, a new Sp1 phosphorylation site Ser702 was defined to be associated with Sp1-HDAC1 interaction and may be important in SR-BI activation, shedding light on the knowledge of delicate mechanism of hepatic HDL receptor SR-BI gene modulation by LDL. PMID: 27320013
  48. findings indicate that WRN interacts with HDACs 1 and 2 to facilitate activity of stalled replication forks under conditions of replication stress. PMID: 27672210
  49. HDAC1- and SRC-mediated phosphorylation of RUNX3 induced by oxidative stress is associated with the cytoplasmic localization of RUNX3 and can lead to RUNX3 inactivation and carcinogenesis. PMID: 27990641
  50. Cutaneous T-cell lymphoma (CTCL) pathogenesis remains unknown, and there are no curative therapies. Our findings not only demonstrate a critical role for IL15-mediated inflammation in cutaneous T-cell lymphomagenesis, but also uncover a new oncogenic regulatory loop in CTCL involving IL15, HDAC1, HDAC6, and miR-21 that shows differential sensitivity to isotype-specific HDAC inhibitors PMID: 27422033

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Subcellular Location Nucleus.
Protein Families Histone deacetylase family, HD type 1 subfamily
Tissue Specificity Ubiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.
Database Links

HGNC: 4852

OMIM: 601241

KEGG: hsa:3065

STRING: 9606.ENSP00000362649

UniGene: Hs.88556

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